Reaction: (R)-pantetheine + H2O = (R)-pantothenate + 2-aminoethanethiol
Other name(s): pantetheinase; vanin; vanin-1
Systematic name: (R)-pantetheine amidohydrolase
Comments: The enzyme hydrolyses only one of the amide bonds of pantetheine. The substrate analogues phosphopantetheine and CoA are not substrates. The enzyme recycles pantothenate (vitamin B5) and produces 2-aminoethanethiol, a potent anti-oxidant [5].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 56093-18-6
References:
1. Duprè, S. and Cavallini, D. Purification and properties of pantetheinase from horse kidney. Methods Enzymol. 62 (1979) 262-267. [PMID: 440106]
2. Duprè, S., Chiaraluce, R., Nardini, M., Cannella, C., Ricci, G. and Cavallini, D. Continuous spectrophotometric assay of pantetheinase activity. Anal. Biochem. 142 (1984) 175-181. [PMID: 6549111]
3. Maras, B., Barra, D., Duprè, S. and Pitari, G. Is pantetheinase the actual identity of mouse and human vanin-1 proteins? FEBS Lett. 461 (1999) 149-152. [PMID: 10567687]
4. Aurrand-Lions, M., Galland, F., Bazin, H., Zakharyev, V.M., Imhof, B.A. and Naquet, P. Vanin-1, a novel GPI-linked perivascular molecule involved in thymus homing. Immunity 5 (1996) 391-405. [PMID: 8934567]
5. Pitari, G., Malergue, F., Martin, F., Philippe, J.M., Massucci, M.T., Chabret, C., Maras, B., Dupre, S., Naquet, P. and Galland, F. Pantetheinase activity of membrane-bound vanin-1: lack of free cysteamine in tissues of Vanin-1 deficient mice. FEBS Lett. 483 (2000) 149-154. [PMID: 11042271]
6. Martin, F., Malergue, F., Pitari, G., Philippe, J.M., Philips, S., Chabret, C., Granjeaud, S., Mattei, M.G., Mungall, A.J., Naquet, P. and Galland, F. Vanin genes are clustered (human 6q22-24 and mouse 10A2B1) and encode isoforms of pantetheinase ectoenzymes. Immunogenetics 53 (2001) 296-306. [PMID: 11491533]
7. Pace, H.C. and Brenner, C. The nitrilase superfamily: classification, structure and function. Genome Biol. 2 (2001) 0001.1-001.9. [PMID: 11380987]